UKL1_ARATH - dbPTM
UKL1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UKL1_ARATH
UniProt AC Q9FKS0
Protein Name Uridine kinase-like protein 1, chloroplastic
Gene Name UKL1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 486
Subcellular Localization Plastid, chloroplast . Cytoplasm . Aggregates in granular precipitates restricted to the cytoplasm, when expressed in transfected cells.
Protein Description Involved in the pyrimidine salvage pathway. The uracil phosphoribosyltransferase (UPRT) activity, that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate, is unsure..
Protein Sequence MPEDSSSLDYAMEKASGPHFSGLRFDGLLSSSPPNSSVVSSLRSAVSSSSPSSSDPEAPKQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLKSGQPYQVPIYDFKTHQRRSDTFRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQYAKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTKLGQHDLCKIYPNVYVIQSTFQIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRSGESMENALRACCKGIKIGKILIHRDGDNGKQLIYEKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVPEAHIIFLNLISAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGTDEEDQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
30PhosphorylationLRFDGLLSSSPPNSS
CCCCCCCCCCCCCCH
33.5423776212
31PhosphorylationRFDGLLSSSPPNSSV
CCCCCCCCCCCCCHH
47.0023776212
32PhosphorylationFDGLLSSSPPNSSVV
CCCCCCCCCCCCHHH
40.7923776212
36PhosphorylationLSSSPPNSSVVSSLR
CCCCCCCCHHHHHHH
30.2223776212
37PhosphorylationSSSPPNSSVVSSLRS
CCCCCCCHHHHHHHH
32.9323776212
40PhosphorylationPPNSSVVSSLRSAVS
CCCCHHHHHHHHHHH
22.8423776212
41PhosphorylationPNSSVVSSLRSAVSS
CCCHHHHHHHHHHHC
19.0523776212
44PhosphorylationSVVSSLRSAVSSSSP
HHHHHHHHHHHCCCC
38.0123776212
47PhosphorylationSSLRSAVSSSSPSSS
HHHHHHHHCCCCCCC
24.9923776212
48PhosphorylationSLRSAVSSSSPSSSD
HHHHHHHCCCCCCCC
28.3923776212
49PhosphorylationLRSAVSSSSPSSSDP
HHHHHHCCCCCCCCC
38.4723776212
50PhosphorylationRSAVSSSSPSSSDPE
HHHHHCCCCCCCCCC
30.6530291188
52PhosphorylationAVSSSSPSSSDPEAP
HHHCCCCCCCCCCCC
44.4123776212
53PhosphorylationVSSSSPSSSDPEAPK
HHCCCCCCCCCCCCC
41.9923776212
54PhosphorylationSSSSPSSSDPEAPKQ
HCCCCCCCCCCCCCC
62.6223776212
481PhosphorylationFGDRYFGTDEEDQ--
CCCCCCCCCCCCC--
30.2729654922

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of UKL1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UKL1_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UKL1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UKL1_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UKL1_ARATH

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.

TOP